Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/70026
DC FieldValueLanguage
dc.contributor.authorHua, Y.W.en_US
dc.contributor.authorChi, M.C.en_US
dc.contributor.authorLo, H.F.en_US
dc.contributor.authorHsu, W.H.en_US
dc.contributor.authorLin, L.L.en_US
dc.date2004zh_TW
dc.date.accessioned2014-06-11T05:59:15Z-
dc.date.available2014-06-11T05:59:15Z-
dc.identifier.issn1367-5435zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/70026-
dc.description.abstractBacillus stearothermophilus leucine aminopeptidase 11 (LAPII) was fused at its C-terminal end with the raw-starch-binding domain of Bacillus sp. strain TS-23 alpha-amylase. The chimeric enzyme (LAPsbd), with an apparent molecular mass of approximately 61 kDa, was overexpressed in IPTG-induced Escherichia coli cells and purified to homogeneity by nickel-chelate chromatography. The purified enzyme retained LAP activity and adsorbed raw starch. LAPsbd was stable at 70degreesC for 10 min, while the activity of wild-type enzyme was completely abolished under the same environmental condition. Compared with the wild-type enzyme, the twofold increase in the catalytic efficiency for LAPsbd was due to a 218% increase in the k(cat) value.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Industrial Microbiology & Biotechnologyen_US
dc.relation.ispartofseriesJournal of Industrial Microbiology & Biotechnology, Volume 31, Issue 6, Page(s) 273-277.en_US
dc.relation.urihttp://dx.doi.org/10.1007/s10295-004-0146-5en_US
dc.subjectleucine aminopeptidaseen_US
dc.subjectBacillus stearothermophilusen_US
dc.subjectamylaseen_US
dc.subjectrawen_US
dc.subjectstarch-binding domainen_US
dc.subjectBacillus sp strain TS-23en_US
dc.subjectthermostabilityen_US
dc.subjectescherichia-colien_US
dc.subjectcyclodextrin glucanotransferaseen_US
dc.subjectexpressionen_US
dc.subjectconstructionen_US
dc.subjectglucoamylaseen_US
dc.subjectgeneen_US
dc.subjectpurificationen_US
dc.subjectadsorptionen_US
dc.subjectproteinsen_US
dc.subjectcloningen_US
dc.titleFusion of Bacillus stearothermophilus leucine aminopeptidase II with the raw-starch-binding domain of Bacillus sp strain TS-23 alpha-amylase generates a chimeric enzyme with enhanced thermostability and catalytic activityen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1007/s10295-004-0146-5zh_TW
item.fulltextno fulltext-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.languageiso639-1en_US-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
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